Trypsin-catalysed formation of pig des-(23-63)-proinsulin from desoctapeptide-(B23-30)-insulin

T. Kubiak, David Cowburn

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Incubation of pig desoctapeptide-(B23-30)-insulin with trypsin in solvent systems consisting of dimethyl sulphoxide, butane-1,4-diol and Tris buffer resulted in the formation of an extra peptide bond between Arg-B22 and Gly-A1 in the DOPI molecule. This DOPI derivative can also be regarded as pig des-(23-63)-proinsulin. The structure of the new, previously unreported, proinsulin analogue was determined on the basis of amino acid analysis, dansylation and digestion with Staphylococcus aureus V8 proteinase. Receptor-binding ability of des-(23-63)-proinsulin was 20% of that of pig desoctapeptide-(B23-30)-insulin and 0.02% of that of pig insulin.

Original languageEnglish (US)
Pages (from-to)665-670
Number of pages6
JournalBiochemical Journal
Volume234
Issue number3
StatePublished - 1986
Externally publishedYes

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Trypsin
Swine
Proinsulin
Tromethamine
Dimethyl Sulfoxide
Peptide Hydrolases
Insulin
Derivatives
Amino Acids
Peptides
Molecules
Staphylococcus aureus
Digestion
desoctapeptide-insulin
des-(23-63)-proinsulin
butane

ASJC Scopus subject areas

  • Biochemistry

Cite this

Trypsin-catalysed formation of pig des-(23-63)-proinsulin from desoctapeptide-(B23-30)-insulin. / Kubiak, T.; Cowburn, David.

In: Biochemical Journal, Vol. 234, No. 3, 1986, p. 665-670.

Research output: Contribution to journalArticle

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